accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
O76064
|
RNF8_HUMAN
|
RING-type E3 ubiquitin transferase RNF8
|
Homo
|
MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQLVSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLCAEQAQQQARVEQLEKTFQEEEQHLQGLEIAQGEKDLKQQLAQALQEHWALMEELNRSKKDFEAIIQAKNKELEQTKEEKEKMQAQKEEVLSHMNDVLENELQCIICSEYFIEAVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKTYSLVLDNCINKMVNNLSSEVKERRIVLIRERKAKRLF
|
E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites . Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity . In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 .
|
O76064
|
Q0ZIZ0
|
PSBH_VITVI
|
Photosystem II 10 kDa phosphoprotein
|
Vitis
|
MATKTVEGSSRSRPKPTTVGELLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISLN
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q0ZIZ0
|
P0DM69
|
TX5_SELPU
|
Toxin OAIP 5
|
Selenotypus
|
MLIVILTCALLVIYHAAAAEELEAKDVIESKALATLDEERFECVLKCDIQYNGKNCKGKGENKCSGGWRCRFKLCLKI
|
Probable ion channel inhibitor. Shows insecticidal activity when injected into mealworms.
|
P0DM69
|
A3QAD1
|
PSD_SHELP
|
Phosphatidylserine decarboxylase beta chain
|
Shewanella
|
MDKLKIALQYIMPKHLLSRLVGKLAAAELGAVTTSVIKWFIKQYKIDMSEAAQSAPEAYASFNQFFTRALKPGIRPLCDDDDYIVHPVDGAVSQCGPIKEGRIFQAKGHEYSSLALLGDQADDAKRFEGGDFATIYLAPKDYHRIHMPIKGTLSKMTYVPGELFSVNPLTAENVPGLFARNERVVAIFETEIGPMAMVLVGATIVASIETVWAGTVTPPTGKKVFTWDYPTEGPEAITLDKGEEMGRFKLGSTVVMLFAKDALEHFADGVEPKAVTRMGQAFAKID
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
|
A3QAD1
|
P14498
|
TRAS2_ECOLX
|
Protein TraS
|
Escherichia
|
MKRSDLEKDAAYILDKFKQLDYEIPSNRQILKVIFYKLVVVYVFQLLFIIFDIFINSNVRDYHYFDTFVITLGSNAFFSLVFLMSTYNLVSLKISLGSEITEQSVLLKLVERKINSYGQFLMVVNAIVGCVLLSSGERFVAGLGFSWFVTYLISMITLQTSLSRYMTPAVVSSLSKVKELLSASPK
|
Involved in surface exclusion.
|
P14498
|
C0HKD6
|
SYWM_CAEEL
|
Tryptophanyl-tRNA synthetase
|
Caenorhabditis
|
MIFSGKFTSHLLNYGFKPNNLRLLSTSTHPTIYFTGIQPTGIPHLGNFFGSIEPWTELQNSVDKNILMMLSVVDQHAISLGPLPANELRQNTHQMTASLIACGVDPNRTLLFRQSDVPQIAQISWILGSLQTTSKLARLPQYKEKKERFKKGDIPVGLLTYPLLQAADVLTFKATTVPVGEDQSQHLNLLGGLAYAFNKTYETEIFPIPKQLTRESHARIRSLREPEKKMSKSSGGPRSRIEITDSRSTIIEKCQKAQSDNAGKVTYDKENRLAVSNLLDLYSAVTKTQTSEIDFSNWTTLDLKMNLAEAVDKRLAPIRQKFEELQNTGEVDKVLTENGEKAREIAEKNLEEIRRTIGFL
|
Catalyzes the attachment of tryptophan to tRNA(Trp).
|
C0HKD6
|
Q62918
|
NELL2_RAT
|
NEL-like protein 2
|
Rattus
|
MESRVLLRTFCVILGLEAVWGLGVDPSLQIDVLSELELGESTAGVRQVPGLHNGTKAFLFQDSPRSIKAPIATAERFFQKLRNKHEFTILVTLKQIHLNSGVILSIHHLDHRYLELESSGHRNEIRLHYRSGTHRPHTEVFPYILADAKWHKLSLAFSASHLILHIDCNKIYERVVEMPSTDLPLGTTFWLGQRNNAHGYFKGIMQDVQLLVMPQGFIAQCPDLNRTCPTCNDFHGLVQKIMELQDILSKTSAKLSRAEQRMNRLDQCYCERTCTMKGATYREFESWTDGCKNCTCLNGTIQCETLVCPAPDCPAKSAPAYVDGKCCKECKSTCQFQGRSYFEGERSTVFSASGMCVLYECKDQTMKLVENAGCPALDCPESHQIALSHSCCKVCKGYDFCSEKHTCMENSVCRNLNDRAVCSCRDGFRALREDNAYCEDIDECAEGRHYCRENTMCVNTPGSFLCICQTGYIRIDDYSCTEHDECLTNQHNCDENALCFNTVGGHNCVCKPGYTGNGTTCKAFCKDGCKNGGACIAANVCACPQGFTGPSCETDIDECSEGFVQCDSRANCINLPGWYHCECRDGYHDNGMFAPGGESCEDIDECGTGRHSCANDTICFNLDGGYDCRCPHGKNCTGDCVHDGKVKHNGQIWVLENDRCSVCSCQTGFVMCQRMVCDCENPTVDLSCCPECDPRLSSQCLHQNGETVYNSGDTWAQDCRQCRCLQEEVDCWPLACPEVECEFSVLPENECCPRCVTDPCQADTIRNDITKTCLDEMNVVRFTGSSWIKHGTECTLCQCKNGHVCCSVDPQCLQEL
|
Required for neuron survival through the modulation of MAPK pathways . Involved in the regulation of hypothalamic GNRH secretion and the control of puberty.
|
Q62918
|
P68030
|
HBG_ALOBE
|
Hemoglobin gamma chain
|
Alouatta
|
MSNFTAEDKAAITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGVKVLTSLGEAIKNLDDLKGTFGSLSELHCDKLHVDPENFRLLGNVLVTVLAILHGKEFTPEVQASWQKMVAGVASALASRYH
|
Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
|
P68030
|
A7H3F3
|
ISPH_CAMJD
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Campylobacter
|
MIIELAKNYGFCFGVKRAIKKAEQIKDAATIGPLIHNNEEISRLQKNFNVKTLENIKSLSNETKAIIRTHGITKQDLEELRKKDIEIFDATCPFVTKPQQICEQMSKEGYEIVIFGDENHPEVKGVKSYVNTKAYVVLDKKELQNIKLPSKIAVVSQTTKKPEHFMEIVNFLMLKAKEVRVFNTICDATFKNQDAIKELSLKSDVMVVVGGKNSANTKQLFLIAKTNCEDSYLIETEEELKKEWFLDKKHCGISAGASTPDWIIQKVIAKIENFGIN
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
A7H3F3
|
P20784
|
ROL6_CAEEL
|
Protein roller-6
|
Caenorhabditis
|
MTLTTATSGAIVFSGATLLVSLFAAASLYSQVSNIWNELDAEIANFRSLTEDMWVDMVKLGAGTASNRVRRQQYGGYGATGVQPPAPTPNPYGGYGASQPAPPEKFPDGIPNGGNQPKFPGGGFPDGPFPNGGGPRGGNQCQCTVENSCPPGPAGPEGEEGPDGHDGQDGVPGFDGKDAEDVQNTPPTGCFTCPQGPLGPQGPNGAPGLRGMRGARGQPGRPGRDGNPGMPGDCGPPGAPGSDGKPGSPGGKGDDGERPLGRPGPRGPPGEAGPEGPQGPTGRDAYPGQSGPQGEPGLQGYGGAAGEDGPEGPPGAPGLPGKDAEYCKCPGREGDAGRSARRHRKFQL
|
Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Involved in body morphogenesis .
|
P20784
|
Q96EY5
|
MB12A_HUMAN
|
Protein FAM125A
|
Homo
|
MDPVPGTDSAPLAGLAWSSASAPPPRGFSAISCTVEGAPASFGKSFAQKSGYFLCLSSLGSLENPQENVVADIQIVVDKSPLPLGFSPVCDPMDSKASVSKKKRMCVKLLPLGATDTAVFDVRLSGKTKTVPGYLRIGDMGGFAIWCKKAKAPRPVPKPRGLSRDMQGLSLDAASQPSKGGLLERTASRLGSRASTLRRNDSIYEASSLYGISAMDGVPFTLHPRFEGKSCSPLAFSAFGDLTIKSLADIEEEYNYGFVVEKTAAARLPPSVS
|
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down-regulation of EGF receptor.
|
Q96EY5
|
A6MM38
|
RR4_BUXMI
|
30S ribosomal protein S4, chloroplastic
|
Buxus
|
MSRYRGPRFKKIRRLGALPGLTSKRPRAGSDLRNQSRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVRIAGKAKGSTGQVLLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITAKDEQKSRALIQNYLDSSPHEELPKHLTLHSFQYKGLVNQIIDSKWVGLKINELLVVEYYSRQT
|
With S5 and S12 plays an important role in translational accuracy.
|
A6MM38
|
A1S3W8
|
TYSY_SHEAM
|
Thymidylate synthase
|
Shewanella
|
MKQYLDLMKHILDKGTDKSDRTGTGTRSVFGYQMRFDLNEGFPLVTTKKCHLRSIIHELLWFLKGETNVDYLHENKVSIWDEWADEKGNLGPVYGAQWRSWPTPDGRHIDQISQVIEQIKATPDSRRLIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLTMMVAQQCNLGLGDFVWTGGDTHLYSNHMEQTQLQLSREPRPLPTMKILRHPESIFDYRFEDFELSGYDPHPHIKAPVAI
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
A1S3W8
|
P59558
|
RL22_BUCBP
|
50S ribosomal protein L22
|
Buchnera
|
METIARHSQARSSAQKLRLVADLIRGKNIEHALNILTFCNKKASILVKKVLKSAISNAEHNHGSDINNLQVKKILIDEGPTMKRMMPRAKGRSDRILKRTSHITIVVSDSKVKDKKGRG
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
P59558
|
C3JZP4
|
RBSD_PSEFS
|
D-ribose pyranase
|
Pseudomonas
|
MKKTPLLNIALSRVIASLGHGDILVIGDAGLPVPPGVELIDLALTQGIPDFISALRIVLSEMQVESHVLAEEILLKQPPALNELNTLSDEAALGERRLVSHEAFKQLSRKARAVVRTGECQPYCNIALVSGVTF
|
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
|
C3JZP4
|
B8D9D7
|
ACP_BUCA5
|
Acyl carrier protein
|
Buchnera
|
MKNIEERIKKIIFEKLDIKQEKIFNDASFIDDLGADSLDTVELIMALEEEFDIEISDEEAEKINTVQKSIDFIQNKNLKK
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
B8D9D7
|
Q8R3I2
|
MBOA2_MOUSE
|
Membrane-bound O-acyltransferase domain-containing protein 2
|
Mus
|
MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAVWFRTYLHSSKTSSFIRHVVATLLGLYLAFFCFGWYALHFLVQSGISYCIMIIAGVESMQQCCFVFALGYLSVCQITRVYIFDYGQYSADFSGPMMIITQKITSLAYEIHDGMFRKDEELTPSQRGLAVRRMPSLLEYVSYTCNFMGILAGPLCSYKDYIAFIEGRASHVAQPSENGKDEQHGKADPSPNAAVTEKLLVCGLSLLFHLTISNMLPVEYNIDEHFQATASWPTKATYLYVSLLAARPKYYFAWTLADAINNAAGFGFRGYDKNGVARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERATFSPTIQTFFLSAIWHGVYPGYYLTFLTGVLMTLAARAVRNNFRHYFLEPPQLKLFYDLITWVATQITISYTVVPFVLLSIKPSFTFYSSWYYCLHVCSILVLLLLPVKKSQRRTSTQENVHLSQAKKFDERDNPLGQNSFSTMNNVCNQNRDTGSRHSSLTQ
|
Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophospholipid leading to the production of a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle . Catalyzes the acylation of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) . Does not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine . Prefers oleoyl-CoA as the acyl donor . May be involved in chondrocyte differentiation .
|
Q8R3I2
|
Q3K5C0
|
MDCG_PSEPF
|
Malonate decarboxylase holo-[acyl-carrier-protein] synthase
|
Pseudomonas
|
MVNTPLAHDLLWGMTPAQLPADAPQWAIDSLAAGQPVVVRRALSEDGCVAVGVRGRFREQRLAAFMSVDSIACRVSPEALCQVESARDLPVMQALRQLRPVLDDCGWTWGVSGSVGFELASGFTAMHERSDLDLILRTPQLITRNQARKLVAYFEQAICRVDLQLQTPFGAVALREWAGNASRVLLKNAREACLVSDPWNPQEQAA
|
Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield holo-[acyl-carrier-protein].
|
Q3K5C0
|
B1VAN0
|
RL11_PHYAS
|
50S ribosomal protein L11
|
16SrXII (Stolbur group)
|
MAKKVVKMVKLQIPAGKANPAPPVGPALGQAQVNIPSFCSQFNETTKDQMGFIIPVIISVYEDRTFTFVTKTPPASDLLKKAAKIDAGSANAKQTKVATISKSQLQEIANLKLRDLNAYSVEQACKIIAGTARNMGILIED
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
B1VAN0
|
B7HPL5
|
HRCA_BACC7
|
Heat-inducible transcription repressor HrcA
|
Bacillus cereus group
|
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITFSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNDEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNILNEKLSGVPMSELHNKIFKEIVTVLRGYVHNYDSAIKILDGTFQVPLSEKIYFGGKANMLSQPEFHDIQKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENSATAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQITDGLKK
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
|
B7HPL5
|
P73451
|
NRTB_SYNY3
|
Nitrate import permease protein NrtB
|
unclassified Synechocystis
|
MASSTAGLRPRRKKNPLSFIYSPKVIRPAVAIAVLLVVWQILCSGEGSNLPSPVQVLEQTYPLILNPFFDNGGTDKGLGIQIFASLTRVAVGFSAAAVVGIALGILIGSSKFMYDALDPIFQVLRTIPPLAWLPIALAALQEAEPSAIFVIFITAIWPIVINTTVGAQQVPQDYRNVSRVLKLSKSQYFFNILFPAAVPYIFTGLRIGIGLSWLAIVAAEMLIGGVGIGFFIWDAYNSSLISEIIIALIYVGIVGLLLDRFIAFLESLVVPAEQK
|
Part of the ABC transporter complex NrtABCD involved in nitrate uptake. The complex is probably also involved in nitrite transport. Probably responsible for the translocation of the substrate across the membrane.
|
P73451
|
Q8PII0
|
YQGF_XANAC
|
Putative pre-16S rRNA nuclease
|
Xanthomonas
|
MPEAGAIRPDGTVLGFDVGSRRIGVAVGSALGAGARAVAVINVHANGPDWVALDRVHKQWRPDGLVVGDPLTLDDKDQPARKRAHAFARQLRERYALPVVLIDERSSSVEAAQRFARERADGRKRRRDAEALDAMAAAVIVERWLAAPDQATLLP
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q8PII0
|
A7GS30
|
METE_BACCN
|
Methionine synthase, vitamin-B12 independent isozyme
|
Bacillus cereus group
|
MALHTSNLGYPRIGLQREWKKTLEAFWAQKIDEQQLITTMKEIHLEHLNVQKEKGIDFIPIGDFTYYDHVLDTAYMLGFIPSRFSNFTSYLDIYFAMARGSKDHVASEMTKWFNTNYHYIVPEYEEGLNISLKDNRPLRLYEEAKRELGIDGKPVILGPYTFLKLAKGYTQDQFPTILHKLIAPYVQLLTELHKAGARLIQIDEPIFVSLTKEEMIEAKKLYEAIQKEVPSANLILQTYFDSVEENYTELITFPVSGIGLDFVHGKEGNIKSIVEHGFPAEKTLAIGCIDGRNIWRANLDEVFALFETLKAHIEPKDWIIQPSCSLLHTPVDKTEETHLSPELFDALAFANQKLEELTLIKRGLSEGVNSIEIEITTYRNSHEAVRSSAARNRKDVQTARASLKEEDFSRPLPFEQRYDLQQKALQLPLLPTTTIGSFPQTPEVRQTRKQWRNGEITNEQYEHFIEQETEKWIRHQENIGLDVLVHGEFERTDMVEYFGERLAGFSFTKNGWVQSYGSRCVKPPIIFGDVAFISDMTVKETVYAQSLTNKVVKGMLTGPVTILNWSFVRNDLPRKEVCYQIALALRHEIERLESSGIRIIQVDEPALREGMPLKEKDWDSYIEWAVQSFRLATASVANETQIHTHMCYSNFEDIVDAIRALDADVISIETSRSHGEFIHTLEQTTYEKGIGLGVYDIHSPRVPSKEEMYTIVEQSLKVCNPKYFWINPDCGLKTRRTEEVLPALEHMVEAAKEARTLLKTNA
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
|
A7GS30
|
O06431
|
DNAJ_NITEU
|
Chaperone protein DnaJ
|
Nitrosomonas
|
MSQSDYYEVLGVGRDADENELKKAYRKLAMKYHPDRNAGDTKAEERFKNIKEAYEILSDPNKRAAYDQFGHAGLNGGMGGAGAQGFSDAFSDIFSDLFGMRGGGRSSVHRGADLRYNLEITLEQAARGAETQIRIPRQEVCDTCHGSGAKPGTSPKTCPTCNGHGQIRMQQGFFSIQQTCSHCQGSGKVVSDPCGDCHGAGWVKRQKTLSVRIPAGVDEGDSIRLTGEGEAGANGGQAGDLYIVIHLASHPVFQREGNHLHCEIPISFTVAALGGEIEVPTLDGHARIKVPAGTQTGKIFRLRSKGITGVRNQSTGDLLCHVAVETPVDLTARQKELLEEFESISQKDGSRHHPRAKSWMEKAREFFAE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
O06431
|
B0BTY6
|
HFQ_ACTPJ
|
RNA-binding protein Hfq
|
Actinobacillus
|
MAKGQSLQDPYLNALRRERIPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPARSVSHNNGGAAHTQQSPAVEAVADKAE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
B0BTY6
|
C4LC89
|
TRPB_TOLAT
|
Tryptophan synthase beta chain
|
Tolumonas
|
MTLLDPFFGEFGGMYSPQILMPVLLELEKAFVDAKDDPEFQAEFQHLLTEYAGRPTPLTLCRNLTKGTKTKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKTRIIAETGAGQHGVATALACALLDLPCRIYMGAVDCERQKPNVFRMRLMGAEVIPVHAGSSTLKDACNEAMRDWTANYKDTHYILGTAAGPHPFPTIVREFQRMIGEEAKEQILKAEGRLPDAVVACVGGGSNAIGMFATFIEEEGVRLIGVEPAGHGIETGKHGAPIGHARKGIYLGMVSFLMQNEDGQVEESHSISAGLDFPSVGPQHAYLSSIGRAQYPSVTDQEALDAFQELSLREGIIPALESSHALAHALKMARSEPEKEQILIVNLSGRGDKDIFTVANALEGEGALS
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
C4LC89
|
B7UWI1
|
HSCA_PSEA8
|
Chaperone protein HscA homolog
|
Pseudomonas
|
MALLQIAEPGQSPKPHERRLAVGIDLGTTNSLVAAVRSGVAEPLPDAQGRLILPSAVRYHAERAEVGESARAAAAEDPFNTVISVKRLMGRGLEDVKQLGEQLPYRFRQGESHMPFIETVQGLKSPVEVSADILRELRQRAETTLGGELVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAVAYGLDKGAEGLVAIYDLGGGTFDISILRLTRGVFEVLATGGDTALGGDDFDHAIAGWVIEEAGLSADLDPGSQRQLLQIACAAKERLTDEASVRVAYGDWSGELSRATLDELIEPFVARSLKSCRRAVRDSGVDLEEIRSVVMVGGSTRVPRVRTAVGELFGCEPLTDIDPDQVVAIGAAIQADALAGNKRGEELLLLDVIPLSLGLETMGGLMEKVIPRNTTIPVARAQEFTTYKDGQTAMMIHVLQGERELVKDCRSLARFELRGIPPMVAGAAKIRVTFQVDADGLLGVSARELSSGVEASIQVKPSYGLTDGEIARMLKDSFDYAGDDKAARALREQQVEAQRLLEAVQSALDVDGERLLDEEERLAIAAQMDTLRELAGGSDTAAIENQIKRLSQVTDAFAARRMDATVKAALSGRRLNEIEE
|
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
|
B7UWI1
|
Q73N90
|
ISPG_TREDE
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Treponema
|
MNSIKLPRTIHIGGKGQVKKLTLGGTSPILLQTMWKESLLGADLLSIVKSLNELEQLGCDIVRFAVPDMDSAEQFVKLTRLTEMPLVADIHFDYKLALRCMDGDTAKIRINPGNIGSKEKTEEVIRKAKDTGTAIRIGVNSGSLPSDLKKKIEEANSKRNLSGDKKALDDEISLLRADTLTEAAARELEIFEKADFKDAVVSMKASNVRETVMANEIFAKKFDNPLHLGVTEAGPLIQGIVKSTIAFYRLLEQNIGSTIRVSLSDSCENEVIAGREILTECGKRQGGIRLISCPRCGRKGFDVQAFVKRWQTKLLSEKKDISIAVMGCVVNGPGEGKHADLGITGAEDSVIIFKHGAITKRLDLKKLTEEEKIKAVDKAFIEELQSL
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q73N90
|
B1WUM4
|
PYRD_CROS5
|
Dihydroorotate oxidase
|
Crocosphaera subtropica
|
MMFNFAQPVYPLVLTAAKNNPENAHQQLLKTLHRLDENRHTVWGKWILENLDHSFTFEDSRLQQNLWGLTFKTPVGLAAGCDKDGLAAGIWDHFGFGFAEIGAVTLHAQPGNPKPRLFRLPQDKAALNRLGANNQGAQKVAQTLKETWQRQPRQIPIGINLCKSKITPLEQAAMDYVGSFRYLEEDADYFVVNVSSPNTPGLRSLQEGEQLNVILQELQSVNSLTKPILVKISPDLSWESIKLIIKLAKTYQLAGIIATNTTIKREGLKTNILEKTGNSIQEEAGGISGQPIRQRSTEVIRFIYEQTQGTLPIIGVGGIFTAEDAWEKITSGASLLQLYTGWIYQGPWCISNINRGLVRKLEKYKLSHISEAVGMDFNS
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
B1WUM4
|
Q8Z118
|
SYV_SALTI
|
Valyl-tRNA synthetase
|
Salmonella
|
MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESKESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGRDAFIDKIWQWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETVLGDTGVAVNPEDPRYKDLIGKFVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAEVFDTKGEESNVYSSEIPAEFQKLERFAARKAIVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDNDGNVYVGRTEDEVRQENNLGADVQLRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQMAEKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEEQDCGFNGGEMTLSLADRWILAEFNQTVKAYREALDNFRFDIAAGILYEFTWNQFCDWYLELTKPVMTGGSESELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVICGITADTIMLQPFPEYNAAQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSEEAVRRVNDNRSFLLNLARLESITVLPADDKGPVSMTKIIDGAELLIPMAGLINKEDELARLAKEVAKIEGEIARIEGKLSNEGFVARAPEAVIAKEREKLDGYAEAKAKLIEQQAVISAL
|
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
|
Q8Z118
|
B3W6P3
|
MNTH_LACCB
|
Divalent metal cation transporter MntH
|
Lacticaseibacillus
|
MASEDKKSKREHIIHFEDTPSKSLDEVNGSVEVPHNAGFWKTLAAYTGPGILVAVGYMDPGNWITSIAGGASFKYSLLSVILISSLIAMLLQAMAARLGIVTGRDLAQMTRDHTSKAMGGFLWVITELAIMATDIAEIIGSAIALKLLFNMPLIVGIIITTADVLILLLLMRLGFRKIEAVVATLVLVILLVFAYEVILAQPNVPELLKGYLPHADIVTNKSMLYLSLGIVGATVMPHDLFLGSSISQTRKIDRTKHEEVKKAIKFSTIDSNLQLTMAFIVNSLLLILGAALFFGTSSSVGRFVDLFNALSNSQIVGAIASPMLSMLFAVALLASGQSSTITGTLAGQIIMEGFIHLKMPLWAQRLLTRLMSVTPVLIFAIYYHGNEAKIENLLTFSQVFLSIALPFAVIPLVLYTSDKKIMGEFANRAWVKWTAWFISGVLIILNLYLIAQTLGFVK
|
H(+)-stimulated, divalent metal cation uptake system.
|
B3W6P3
|
P23028
|
PA2HD_PSETE
|
Acidic phospholipase A2 homolog textilotoxin D chain
|
Pseudonaja
|
MHPAHLLVLLGVCVSLLGAASIPRPSLNIMLFGNMIQCTIPCEQSWLGYLDYGCYCGSGSSGIPVDDVDKCCKTHDECYYKAGQIPGCSVQPNEVFNVDYSYECNEGQLTCNESNNECEMAVCNCDRAAAICFARFPYNKNYWSINTEIHCR
|
Snake venom oligomeric phospholipase A2 that has potent presynaptic neurotoxicity. Chain D is not itself neurotoxic, but it is essential for the neurotoxicity of textilotoxin. Chain D possesses a very low phospholipase activity.
|
P23028
|
Q9D0V8
|
CINP_MOUSE
|
Cyclin-dependent kinase 2-interacting protein
|
Mus
|
MEAKTLGIATPRKPVLSVSARKLKDNAADWHNLILKWDSLSDKGFTTASSIANLKVSLLSKEKVELESSSPASMEEEEKTNLDYDKGLEALCEELQAILDGLTKIQMKMEKLSSTTKGICELENYHYREESSRPPLFHTWPTAFFYEVSRRLSEAYKKELLLKHTIGAELAHTADRNLSLTYLSMWLHQPYIESNSKLQLESMLLETGHRAL
|
Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling in response to DNA damage. Also involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles. Promotes maturation of pre-60S ribosome together with SPATA5, SPATA5L1 and C1orf109.
|
Q9D0V8
|
A9CKB4
|
4HYPE_AGRFC
|
4-hydroxyproline 2-epimerase
|
Agrobacterium tumefaciens complex
|
MRWKRTLQLLDVHCEGEIGRVVTGGAPKIPGNTVAEQLHWMNTDPQGEALRRFLTLEPRGTPMGSVDLLLPPKHPDAHAAFVILQPDQAHASSGSNSICATTALLESGMVEMQEPETVIILETAAGLVKATATCRDGRCEKVKLTMVPSFVHELDVSIDTPEWGRVTMDISYGGIFYALVDVRQIGLTIEKANAAKLVAAGMTLKDLVNREMTVVHPEIPAISGVAYVMFRDVDADGSIRTCTTMWPGRADRSPCGTGNSANLATLYARGKVKVGDEYKSRSIIGSEFDVGLSAVTEVAGRPAVIPTIAGRGFTFGLHQVGLDPFDPLGDGFAMTDVWGPEAGNI
|
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp, which would allow A.tumefaciens to grow on t4LHyp as a sole carbon source. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.
|
A9CKB4
|
A3RLD7
|
CRGB_MACMU
|
Gamma-B-crystallin
|
Macaca
|
MGKITFYEDRAFQGRSYECTTDCPNLQPYFSRCNSIRVESGCWMIYERPNCQGHQYFLRRGEYPNYQQWMGLSDSIRSCHLIPPHSGTYRMKIYERDELRGQMSELTDDCLSVQDRFHLTEIHSLNVLEGSWILYEMPNYRGRQYLLRPGEYRRFLDWGAPNAKVGSLRRVMDLY
|
Crystallins are the dominant structural components of the vertebrate eye lens.
|
A3RLD7
|
A2BQ41
|
HIS1_PROMS
|
ATP phosphoribosyltransferase
|
Prochlorococcus
|
MITIALPKGALLKDSISTFKKAGLDFSNALEENNRSLTFESNCKRAKALLVRNGDVPVYVSYGQADLGIVGYDVLRESELKVAKLLDLGFGGCHMSLAVKKNSNYLKPTDLPANCKVASKFIKTARSYFEELNIPVEIVHLTGSVELGPITGMAEAIVDLVATGKTLKENGLIKIDDLYYSTARLIGNPLSMRLDDNHLRDTILSIESTNAL
|
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
|
A2BQ41
|
Q8EK71
|
EFG1_SHEON
|
Elongation factor G 1
|
Shewanella
|
MARTTPIERYRNIGICAHVDAGKTTTTERVLFYTGLSHKIGEVHDGAATTDWMVQEQERGITITSAAVTTFWRGMDAQFTEHRINIIDTPGHVDFTIEVERSLRVLDGAVVVFCGASGVEPQSETVWRQADKYRVPRIVFVNKMDRAGADFERVVKQIRTRLGATCVPIQLNIGAEENFTGVIDLIKMKAINWNEADQGMTFSYEAIPAHLTAKAEEMHEFLVEAAAEASDELMDKYLEEGTLSEEEIKKALRQRTINNEIVLATCGSAFKNKGVQAVLDAVVEFLPAPVDVPPIKGIDDNEQEVERPSDDNAPFAALAFKIATDPFVGTLTFIRVYSGVLESGSGVYNSVKQKRERIGRIVQMHANDRTELKEVRAGDIAAAIGLKEVTTGDTLCDNDHKVILERMEFPEPVITIAVEPKSKADQDKMGIALQKLAAEDPSFRVETDEESSQTLISGMGELHLDIIVDRMRREFGVECNVGKPQVAYRETIRGSVEAEGKFVRQSGGRGQFGHVWLKLEPNEEGAGYEFINAIVGGVVPREFIPAVDKGIQEQMKNGVLAGFPVLDVKVTLFDGSYHDVDSNEMAFKIAGSMGFKKGALEAKPVLLEPCMKVEVTTPENYMGDVVGDLNRRRGLIEGMDDGFGGIKIIHAVVPLSEMFGYATDLRSATQGRASYSMEFLKYTDAPQNIAKAIIESRS
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
Q8EK71
|
Q44906
|
FLIQ_BORBU
|
Flagellar biosynthetic protein FliQ
|
Borreliella
|
MTAGHILYLIRISIENIIILSAPMLIIALIVGLLISIFQAITSIQDQTLSFIPKIIVILLVIVIFGPWILNKLMQFTYMIFSQLQNV
|
Role in flagellar biosynthesis.
|
Q44906
|
A6T228
|
HEMH_JANMA
|
Protoheme ferro-lyase
|
Janthinobacterium
|
MSFRTEPPYIHGSTPKTAVVLVNLGTPDAPTTSAVRRYLKQFLSDPRVVEIPRAIWWFILHLVILPFRSGQSAKKYASIWSNEGSPLKVHTEKQAKLLNGYLGERGHKVKVVYAMRYGQPALPDVLRQLKADGCERILFLPAYPQYSGTTTASIFDAVFSHYTQERNVPELRFIKHYHDHDAYIRALRKSVQAHWDMAGRPDKLVMSFHGVPKRTLTLGDPYHCECHKTARLLAKELELTQEQYMVTFQSRFGKAEWLQPYTAPTLQKLAKEGIGRVDVICPGFTSDCLETLEEIAMEARHDFMSAGGKDFNYIGCLNEDDAWIKAMAEITELHLIGWPTIVPPSLREEQEQQAHISREEARRLGADQ
|
Catalyzes the ferrous insertion into protoporphyrin IX.
|
A6T228
|
Q9JX02
|
RL11_NEIMA
|
50S ribosomal protein L11
|
Neisseria
|
MAKKIIGYIKLQIPAGKANPSPPVGPALGQRGLNIMEFCKAFNAATQGMEPGLPIPVVITAFADKSFTFVMKTPPASILLKKAAGLQKGSSNPLTNKVGKLTRAQLEEIAKTKEPDLTAADLDAAVRTIAGSARSMGLDVEGVV
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
Q9JX02
|
Q70RW3
|
CYB_HYPAP
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Hyperoodon
|
MINIRKTHPLMKIINNTFIDLPTPSNISSWWNFGSLLGLCLITQILTGLFLAMHYTPDTTTAFSSIAHICRDVNYGWVIRYLHANGASMFFICLYAHIGRGLYYGSYIFLETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFALHFILPFIILALAIVHLLFLHETGSNNPTGIPSDMDKIPFHPYYTIKDTLGALLLILVLLTLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILLFIPLLHTSKQRSMMFRPFSQLLFWLLIADFLTLTWIGGQPVEHPYMIMGQLASMLYFLLILVLMPMASLIENKLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q70RW3
|
B6JP93
|
TSAD_HELP2
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Helicobacter
|
MILSIESSCDDSSLALTRIKDAQLIAHFKISQEKHHSSYGGVVPELASRLHAENLPLLLERIKISLNKDFSKIKAIAITNQPGLSVTLIEGLMMAKALSLSLNLPLILEDHLRGHVYSLFINEKQTCMPLSVLLVSGGHSLILEARDYENIKIVATSLDDSFGESFDKVSKMLDLGYPGGPIVEKLALDYRHPNEPLMFPVPLKNSPNLAFSFSGLKNAVRLEVEKNAPNLNDEVKQKIGYHFQSAAIEHLIQQTKRYFKTKRPKIFGIVGGASQNLALRKAFENLCDAFDCKLVLAPLEFCSDNAAMIGRSSLEAYQKKRFVPLEKANISPRTLLKSFE
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
B6JP93
|
Q8CTP4
|
LARC_STAES
|
Nickel-pincer cofactor biosynthesis protein LarC
|
Staphylococcus
|
MTKALYLDCHAGIAGDMLLSALVDLGANPEDIESELKKLPLDQFKLHFQKRVKQGIHAMTLNIDVKEANHHRHVNDIFKMIDDSTLPERVKYRSKKIFEIIGQAEAKIHGMSFEEVHFHEVGAMDSIIDIIGGCIALEQLGINTLYCSAIPTGHGKINIAHGIYPIPAPATAEILKGIPIAHFDVQSELTTPTGAAFAKGLVSSFGPFPSATIQHIGYGAGSKDFDFPNILRVIQFESEFEQQDSVQVIECQIDDMTPEALGYFMNNALEQGALDAYYTPIFMKKSRPSTQLTLICKLHDKTYFEQLILQETSSLGVRSTSVNRKTLNRAFKILSTQHGTVSIKFGLQNGKIMKMKPEYEDLKKIAKTTKQPFQVIHNEVLQQLYQTYHIGNILQ
|
Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent enzymes.
|
Q8CTP4
|
Q5FQB4
|
GLMM_GLUOX
|
Phosphoglucosamine mutase
|
Gluconobacter
|
MATKRSLFGTDGIRGTANTAPMTVEIAQRLGQAAGLYFMRSQNRRHSVVLGKDTRLSGYMLECALVAGFLSAGMDVILVGPLPTPAIAMLTRSLRADLGVMVSASHNPFTDNGIKLFGPDGFKLSDEVEGEIEDLMSQDLSARLASPAQIGRASRLTDAAGRYIENAKASFPRGLRLDGLKIVIDCANGSAYRVAPTALWELGAEVIKIGCSPDGLNINDGVGSTHPETLCAAVREHGADFGIALDGDADRVLIADENGNLVDGDQIIGLIAAFWKQHDRLRGNTVVTTVMSNMGLEKALAENGLELQRTAVGDRYVVERMREIGANLGGEQSGHMVLSDYATTGDGLIAALQVLAVSVETKRPASEICRFFTPYPQLLKNVRYSGTSPMSSPDLAAAKAWADERLAGSGRLVLRASGTEPLIRVMAEAQDEALVHEVVDHVCDVIRAIAHA
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q5FQB4
|
A7VN14
|
MSMB2_PROFL
|
Small serum protein 2
|
Protobothrops
|
MRVFFSLIIFSFMLATCQGACGIGPLVSSPTDAMAPKKCVDPNDRRKHLIVSTWNTADCLRCECDNDGLSCCHRYGGLAERAGCKSVLNQVTCEYEFYRLDDLSKRCDA
|
May serve as a self-defense protein against the toxic effects of the snake venom during accidental envenomation. Does not show inhibitory activity towards brevilysin H6.
|
A7VN14
|
Q5YYB6
|
IDI_NOCFA
|
Isopentenyl pyrophosphate isomerase
|
Nocardia
|
MPVELVDEAGRAVGACPVAEAHRDPGKLHRAFSVLLFDTAGRVLLQQRAAVKTRFPLLWANTCCGHPAPGESVEAAAATRLAEELGVAAGLTEVGVFRYRAADTATGRVEHEWDHVLIGTLDTTPHPDPAEVANLRWVRPAEVRAKLAAEPAAYTPWLAEVLEIADAAYRESAGR
|
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
|
Q5YYB6
|
Q41005
|
CBPX_PEA
|
Serine carboxypeptidase-like
|
Pisum
|
TGESYAGHYIPALASRIHQGNQANEGIHINLKGLAIGNGLTNPAIQYKGYPDYALDMGIITQTTHDLLGKVLVPACELAIKLCGTNGKVSCLTANVACNLIFSDIMLHAGGVNYYDIRKKCEGSLCYDFSNMEKFLNQESVRDSLGVGKIRFVSCSTEVYMAMLVDWMRNLEVGIPLLLEDGINLLIYAGEYDLICNWLGNSRWVHAMKWSGQKEFVASSDVPFVVNGSQAGLLKSYGPLSFLKVHDAGHMVPMDQPKAALEMVKQWTRGTLAESIDGEEKLVADM
|
Involved in degradation of small peptides.
|
Q41005
|
Q8Z9A6
|
DXR_SALTI
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Salmonella
|
MKQLTILGSTGSIGCSTLDVVHHNPDSFRVIALVAGKNVARMAEQCLEFSPRYAVMDDTSSAEQLKIMLQQHGSRTEVLSGQQAACEMAALDEVGHVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDEVKRSNARLLPVDSEHNAIFQSLPQSIQHNLGYADLEQNGVTSILLTGSGGPFRETPMCDLAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASARQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVTSGAQPLDFCKLSALTFSAPDYQRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAGLNLAVLERMDLHEPASVDDVLQVDAIAREVARKQVIRLSR
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q8Z9A6
|
A4XXN9
|
RSMJ_PSEMY
|
rRNA (guanine-N(2)-)-methyltransferase
|
Pseudomonas
|
MTDEPRNASIRMDALQAHHAEAAARWATRLGLPRVGETDFALQLGDQGLQLVELGDKAPGPVRVDFVEGAAAHRRQFGGGSGQMIAKAVGVQSGIRPRILDATAGLGRDAFVLASLGCEMTLIERQPLIAALLEDGLQRAELDLEVAPIAARMRLLTGNAIDLMQNWQGEAPQVIYLDPMFPHRDKSALVKKEMRLFRPFVGDDLDAPALLAAALALASHRVVVKRPRKAPAIEGTKPGYVLEGKSSRYDVYPKKKLEGA
|
Specifically methylates the guanosine in position 1516 of 16S rRNA.
|
A4XXN9
|
A4XL26
|
HIS1_CALS8
|
ATP phosphoribosyltransferase
|
Caldicellulosiruptor
|
MVTIALPKGRLTEEATELFQRSSLISIDISQETRKLVLEDPRGNLRFLMVKPFDVPTYVEYGIADMGIVGKDVLLEVNKKVYELLDLKIGKCFIALAGPKGLREELLKKPEKIIATKFPNITKEYFENVLGEDVQIIKLNGSVELAPILGLSDMIVDIVESGRTLRENGLEVYEKLYDISARLIINRASLKLKREIEGIVNCLERMILQ
|
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
|
A4XL26
|
A5DG70
|
GUF1_PICGU
|
Ribosomal back-translocase
|
Meyerozyma
|
MYIHSSRTVLARYGSRTPLLRPSVLGRYSTSPAATIEARKIALNRDNYIKSVYDRIAKIPPENYRNFSIVAHVDHGKSTLSDRLLELTGVIQPGDKNQVLDRLDVERERGITVKAQTCTMIFNDPRNGQDYLLHLVDTPGHVDFRAEVSRSYASCGGALLLVDATQGVQAQTVANFYLAYSMGLKLIPIINKIDLDAADIPRAMDQVESTFELDRENCLQVSAKTGLNVKSILPAIVDHIPAPDCDINSPLKALLVDSWHDPYVGVVMLLYVKEGTIKKGMKLLSAHTEGRYEVKEVGIMYPDKVPMESIRAGQVGYIVPGMKDPSQAKIGDTFFQYGKHEGLEALPGFEEPKPMVFVGAFPAEGSEFKVMDDHIANLVLNDRSVTLEKETSNALGLGWRLGFLGSLHASVFQERLENEYGAKIILTAPTVPYKIVYKDGTDKIVTNPDEFPGSDLRNQNVDKLMEPYVNAIMTIPDEYIGAVMSLCENNRGIQKELEYLTNGQVLMRYEIPLAQLVEDFFGKLKGCTKGYASLDYEDAGYKKSDIVKMELCVNGEPQDALTQVMHRSQVQARGKEYVVRFKEYLRFQLFEVAIQAKVNNKVVARETIKAKRKDVTQKLHAADISRRKKLLSRQKEGKKQMKASGRVHINHEAYQAFLRRTI
|
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
|
A5DG70
|
A1JTD7
|
RSMG_YERE8
|
16S rRNA 7-methylguanosine methyltransferase
|
Yersinia
|
MLKKLDSLLSAAGIELPDQQKHQLIGYVELLDKWNKAYNLTSVRDPMQMLVRHILDSIVVNPHLQGSRFIDVGTGPGLPGIPLAIVRPDAHFVLLDSLGKRVRFLRQVQHELGLSNIEPVQSRVEDFAAKPPFDGVISRAFASLQDMLSWCHHLPAKPEGRFYALKGVRPDDELATLPEGIVVESVVRLRVPELDGERHLVILKSN
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
A1JTD7
|
Q1REM0
|
KDPB_ECOUT
|
Potassium-translocating ATPase B chain
|
Escherichia
|
MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASDVMPGNALFSAAISGWLWVTVLFANFAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEASDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLWPFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASEFIPAQGVEEKALADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDAIRRHVEANGGHFPADVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMRLHSPDSAILSAVIFNALIIVFLIPLALKGVSYKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
|
Q1REM0
|
Q82QN1
|
Y474_STRAW
|
Putative S-adenosyl-L-methionine-dependent methyltransferase SAV_474/SAV474
|
Streptomyces
|
MTDEQERVQPSGVWATAVGVARVRALETERENALFRDPLAQAFATAGGLWPSSPPLPDDEAARRRRLTVSFSIVIRTKFLDDLLQQASASGVRQVVLLGAGMDSRAFRMDWPEGTRLFEVDTAAPLDFKASVLRQERADARCERITVAVDLREDWPGALAAVGHDPAVPTVWIAEGLLIYLPEDAVELLLARISAQSAAGSRMGLTLGSRGVIERFGADAAPGSAASMWVSEMPDDPVGWLAGHGWEADSHTLRERAAAYGRPISTPPQREERPGGLISAVRR
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q82QN1
|
Q99ZD0
|
PFKA_STRP1
|
Phosphohexokinase
|
Streptococcus
|
MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGMEVYGINRGYAGMVDGDIFPLGSKEVGDKISRGGTFLYSARYPEFAQLEGQLAGIEQLKKHGIEGVVVIGGDGSYHGAMRLTEHGFPAVGIPGTIDNDIAGTDYTIGFDTAVNTAVEAIDKLRDTSSSHGRTFVVEVMGRNAGDIALWAGIASGADQIIVPEEEFDIEKVASTIQYDFEHKGKNHHIIVLAEGVMSGEAFAQKLKEAGDKSDLRVTNLGHILRGGSPTARDRVIASWMGSHAVELLKDGKGGLAVGIHNEELVESPILGTAEEGALFSLTEEGKIIVNNPHKARLDFAALNRSLSQ
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
Q99ZD0
|
P25672
|
3L24_NAJNA
|
Toxin D
|
Naja
|
IRCFITPDITSKDCPNGHVCYTKTWCDGFCRIRGERVDLGCAATCPTVKTGVDIQCCSTDDCDPFPTRKRP
|
Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.
|
P25672
|
P68046
|
HBB_ODORO
|
Hemoglobin beta chain
|
Odobenus
|
VHLTADEKAAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFDSFGDLSSPDAVMGNPKVKAHGKKVLNSFSDGLKNLDNLKGTFAKLSELHCDKLHVDPENFKLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P68046
|
Q5R530
|
NXPH1_PONAB
|
Neurexophilin-1
|
Pongo
|
MQAACWYVLLLLQPTIYLVTCANLTNGGKSELLKSGSSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG
|
May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors.
|
Q5R530
|
P75250
|
IPYR_MYCPN
|
Pyrophosphate phospho-hydrolase
|
Mycoplasma
|
MDKFLIDVTVEIPKSSKIKYEYDRKTSQIRVDRILFGSESYPQNYGFIANTLDWDGDELDCFIFADQAFLPGVVVPTRIVGALEMVDDGELDTKLLGVIDCDPRYKEINSVNDLPKHRVDEIIGFLKTYKLLQKKEVIIKGVQSLEWAKKEYQVCVDLMKQYGKLPKDEFIAKMQKLHPEHYQK
|
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
|
P75250
|
Q9TDK2
|
CYB_DELCT
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Delphinus
|
MTNIRKTHPLMKILNDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTSTAFSSVAHICRDVNYGWFIRYLHANGASMFFICLYAHIGRGLYYGSYMFQETWNIGVLLLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALAAVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGALLLILTLLALTLFTPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILIFIPMLQTSKQRSMMFRPFSQLLFWTLVADLLTLTWIGGQPVEHPYIIVGQLASILYFLLILVLMPTAGLIENKLLKW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q9TDK2
|
Q2RJM0
|
RS15_MOOTA
|
30S ribosomal protein S15
|
Moorella
|
MALDAAKKREIIARYQKHENDTGSPEVQIAILTERINHLTEHLQVHHKDHHSRRGLLKMVGQRRGLLNYLRENDVERYRQIVESLGLRR
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
Q2RJM0
|
A7ZHS1
|
LPXA_ECO24
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Escherichia
|
MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRGLIR
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
A7ZHS1
|
Q6FZS8
|
GATC_BARQU
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
|
Bartonella
|
MSVDQETVKRVSHLARIAIHDDEIEPMTKELNVILGFVEQLNEVDVNGIEPLTSVMPMALRMREDSVTDGDKVADIVANAPVTEENFFLVSKVVE
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
Q6FZS8
|
Q07V68
|
MIAB_RHOP5
|
tRNA-i(6)A37 methylthiotransferase
|
Rhodopseudomonas
|
MDQPRKLHIKSFGCQMNVYDAQRMVDALAPEGFVETQSADDADLVILNTCHIREKAAEKVYSELGKLRLLKQDAASHGRRFEIAVAGCVAQAEGAEIIRRQPAVDVVVGPQSYHHLPELLEKARRDGRALETEFPIEDKFGVLPPPRPDAIRARGVSAFVTVQEGCDKFCSFCVVPYTRGAEMSRPVAKILDDVKRLIDNGVREITLIGQNVNAYHGEGPDDRPWTLGALLRHLASVPGVARLRYSTSHPLDVDDELIAAHRELPGLMPFVHLPVQSGSDAILAAMNRRHSADDYRRVIDRFRQADPSIAFSSDFIVGFPGETDRDFEATLALVTQIGYAGAYSFKYSPRPGTPAAELQEMVAPAVMDQRLEQLQGLIDSQQAAFNRASIGTTVDVLFERAARHPGQIVGRTAYLQPAHVMAADDIVGQVLPVTIHSLERYSLIGELVKPQPARPPKPLPVTTGA
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
Q07V68
|
Q03745
|
CR1EB_BACTA
|
Insecticidal delta-endotoxin CryIE(b)
|
Bacillus cereus group
|
MENNIENQCIPYNCLNNPEVEILGIERSNSNVAAEIGLGLSRLLVSRIPLGDFILGLFDVIWGAIGPSQWDIFLEQIELLIGQRIEEFARNQAISRLQGLSNLYRIYTNAFKNWEVDPTNPALREEMRIQFNDMNSALTTAIPLFSVQGYEIPLLSVYVQAANLHLSVLRDVSVFGQRWGFDVATINSRYNDLTRLIGEYTDYAVRWYNTGLNRLPRNEGVRGWARFNRFRRELTISVLDIISFFQNYDSRLYPIPTIYQLTREVYTDPVINITDYRVTPSFESIENSAIRSPHLMDFLNNIIIDTDLIRGVHYWAGHRVTSHFTGSSQVISSPQYGITANAEPSRTIAPSTFPGLNLFYRTLSDPFFRRSDNIMPTLGINVVQGVGFIQPNNGEVLYRRRGTVDSLDELPIDGENSLVGYSHRLSHVTLTRSLYNTNITSLPTFVWTHHSATDRNIIYPDVITQIPLVKSFSLTSGTSVVRGPGFTGGDIIRTNVNGNVLSMSLNFSNTSLQRYRVRVRYAASQTMVMRVNVGGSTTFDQGFPSTMSANGSLTSQSFRFAEFPVGISTSGSQTAGISISNNPGRQTFHLDRIEFIPVDATFEAEYDLERAQKAVNSLFTSSNQIELKTDVTDYHIDQVSNLVDCLSDEFCLDEKRELSEKVKHAKRLSDERNLLQDPNFRGINRQPDRGWRGSTDITIQGGDDVFKENYVTLPGTFDECYPTYLYQKIDESKLKAYNRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSVESPIGRCGEPNRCVPHLEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLQEDLGVWVVFKIKTQEGYARLGNLEFIEEKPLIGEALSRVKRAEKKWRDKREKLQLETKRVYTEAKEAVDALFVDSQYDRLQADTNIGMIHAADRLVHQIHEAYLPELPFIPGINVVIFEELENRISTALSLYDARNVIKNGDFNNGLSCWNVKGHVDVVEQNNHRSVLVVPEWEAEVSQTIRVCPGRGYILRVTAYKEGYGEGCVTIHEIENNTDELKFKNCEEEEVYPTDTGTCNDYTAHQGTAGSTDSCNSRNIRYEDAYEMNTTASVNYKPTYEEERYTDVQGDNHCEYDRGYVNYRPVPAGYVTKELEYFPETDKVWIEIGETEGKFIVDNVELLLMEE
|
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.
|
Q03745
|
A9I7J3
|
CCME_BORPD
|
Heme chaperone CcmE
|
Bordetella
|
MTPQRKRRLVMLAALAGGVGVAVALALAALQQNINLFYSPSQIAAGEAPLHTRIRAGGLVQDGSLRRAPDSLAVQFGITDGVQQVLVRYDGILPDLFREGQGIVALGKLDAQGMLQADEVLAKHDQNYMPPEAAHALKQGAATSGGTPAAEPQP
|
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
|
A9I7J3
|
B3PVT4
|
AROE_RHIE6
|
Shikimate dehydrogenase (NADP(+))
|
Rhizobium
|
MGDSRETFGPKAFVTGFPIKHSRSPLIHGYWLKTLGLPGSYRAHEVAPEAFADFIASLKDGSSGFAGGNVTIPHKELAFRLADRPDALSQELGASNTLWLEDDLLHATNTDGRGFTANLDERHPGWDRHDTAVIFGAGGASRAIIQAVRDRGFKTIHVVNRTVGRARELADRFGPKVHAHPAGALAEVMKGAGLFINTTSLGMDGEAAPQLDFTPLTADAVVTDIVYVPLKTPLLAQAQEQGFPIVDGLGMLLHQAVPGFEKWFGKRPVVDAALRALIIADMEAH
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
B3PVT4
|
Q8XXF5
|
RNPH_RALSO
|
tRNA nucleotidyltransferase
|
Ralstonia
|
MRPSGRQPDQLRPVTLTRHYTRHAEGSVLVCFGDTHVLCTASVLPKVPPHKKGSGEGWVTAEYGMLPRSTHTRSDREAARGKQSGRTQEIQRLIGRAMRSVFDLSALGEHTIHLDCDVLQADGGTRTASITGAFVAAHDAISVMRKKGQLTGEPIRDFVAAVSVGVVDGVPVLDLDYPEDASCDTDMNIVMTGAGGFVEVQGTAEGTPFTRTEMDALLGLADHGIRTLIGLQKQALGL
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
Q8XXF5
|
Q47AZ9
|
UBIC_DECAR
|
Probable chorismate pyruvate-lyase
|
Dechloromonas
|
MKRSKWRTRFAGAYCDPILRSWLTEPDSLTARCQRASSAFRVRLLRYGKGQALADEAVEGKAGRHSAWVREVVLECDGVPVIFAHTTLSTARRGRMTRWMAGLGSRSLGSLLFAYPGFKRGGIEFLRLDRCHPLYRRAAALGAGRKSLWARRSLHRLGGQQVLVTEVFLPAITLLK
|
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
|
Q47AZ9
|
Q6FKS8
|
SPB4_CANGA
|
ATP-dependent rRNA helicase SPB4
|
Nakaseomyces/Candida clade
|
MGKSLEWADLDYELQPWIKKAINVSGFDSMTPVQASTIPMFAKNKDVVVESVTGSGKTIAFVIPILEKIISEGINNSKFKKGHFYSLILAPTRELSMQIQNVVSSFLEHYPEDQYPIRSQLVVGTNEKSVRDDVNTLLDERPQILIGTPGRVLDFLQSPSVKTSSCGMVVLDEADRLLDVSFFKDVEKILNVLPKQRRTGLFSATISSAGTLIFKTGLRNPVKITVNSQGKNAPTTLNLFYSVMKPEEKLQNLIHIMNNIRFKKCIVYFSTCVSVTFFYQYLKYLQQTDKTLREDLQVISIHGKLTTQSRRKALSTFTESLSDCILLTTDVAARGIDIPDVDLVLQIDPPTDADIFLHRCGRTGRANKIGRAIVFLNEGREEDYIPFMEVKNVDIEETDINKNKISNDNNDEFYQRFTKWLLSDRANYDLSVKSYVAFIRYYSKHSATSIFRLQSLDYVSLGKMYGLFRLPRMPEITKYLQDKEKSGETVVGYYGEGWLMNPPPIDMDKYAYQDKKREKARIEELKNLAQINDKKKLKAELKKKNMAWSSKTMTKEERQERRKKLDLKRKAIELEIAAEAERDESDTEITQDWKDEILQKKKKKKVGSEMQGSFDDL
|
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
|
Q6FKS8
|
P24823
|
PPBN_MOUSE
|
Embryonic-type alkaline phosphatase
|
Mus
|
MWGACLLLLGLSLQVCPSVIPVEEENPAFWNRKAAEALDAAKKLKPIQTSAKNLVILMGDGMGVSTVTATRILKGQQQGHLGPETQLAMDRFPHMALSKTYNTDKQIPDSAGTGTAFLCGVKTNMKVIGLSAAARFNQCNTTWGNEVVSVMHRAKKAGKSVGVVTTTSVQHASPAGTYAHTVNRGWYSDAQMPASALQDGCKDISTQLISNMDIDVILGGGRKFMFPKGTPDQEYPTDTKQAGTRLDGRNLVQEWLAKHQGARYVWNRSELIQASLNRSVTHLMGLFEPNDMKYEIHRDPAQDPSLAEMTEVAVRMLSRNPKGFYLFVEGGRIDHGHHETVAYRALTEAVMFDSAVDKADKLTSEQDTMILVTADHSHVFSFGGYTQRGASIFGLAPFKAEDGKSFTSILYGNGPGYKLHNGARADVTEEESSNPTYQQQAAVPLSSETHSGEDVAIFARGPQAHLVHGVQEQNYIAHVMAFAACLEPYTDCGLASPAGQSSAVSPGYMSTLLCLLAGKMLMLMAAAEP
|
Alkaline phosphatase that can hydrolyze various phosphate compounds.
|
P24823
|
A6W572
|
UPP_KINRD
|
UPRTase
|
Kineococcus
|
MRLSVIDHPLVAHKLTALRDARTDSPTFRRLADELVTLLAYEATRDVAVEPHPVTTPVTATTGVRLTSPKPIVVPILRAGLGMLDGMVRLLPTAEVGFLGMIRDETTLQATTYANRLPDDLSGRQVFVLDPMLATGGTLVAAITYLLERGARDVTALCLLAAPEGLEVVRTAFDDHAQVTVVTAAVDERLDENGYIVPGLGDAGDRLYGVV
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A6W572
|
O94229
|
IDH1_KLULA
|
NAD(+)-specific ICDH
|
Kluyveromyces
|
MLRQGIAAQKKSFATLAAEQLLPKKYGGRYTVTLIPGDGVGKEVTDSVVKIFENENIPIDWETIDISGLENTENVQRAVESLKRNKVGLKGIWHTPADQTGHGSLNVALRKQLDIFANVALFKSIPGVKTRLNNIDMVIIRENTEGEYSGLEHESVPGVVESLKIMTRAKSERIARFAFDFALKNNRKSVCAVHKANIMKLGDGLFRNTVNEIGANEYPELDVKNIIVDNASMQAVAKPHQFDVLVTPNLYGSILGNIGSALIGGPGLVPGANFGREYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLRHLGLNAYADRISKATYDVISEGKSTTRDIGGSASTSEFTNAVIEKLAKL
|
Performs an essential role in the oxidative function of the citric acid cycle.
|
O94229
|
Q2P472
|
DXS_XANOM
|
1-deoxyxylulose-5-phosphate synthase
|
Xanthomonas
|
MIDTTRYPRLSRIHTPDDLRRFDEAELTVIAEELRSYLIESVGKSGGHFAAGLGVIELTVALHYLYQTPVDQLVWDVGHQTYPHKILTGRRDQIHTVKQKDGVAPFPKREESVYDTFGVGHSSTSISAALGMAIAAQRNGDDRKVVAVIGDGAMTAGMVYEALNHAGGMDPEPNLLVILNDNRMSISEAVGGLTKMLGRASGSRTLNAIREGGKKILGDKKNNPTARFVRRWEEHWKGMFVPSTLFEEMGFHYTGPIDGHDLPRLVGALKTLQTLKGPQLLHVITTKGKGYELAEGDQIGYHAVSPFDPSKGLVAKGGAKKPTYTDVFSDWVCDMAAAEPKLLVITPAMREGSGLVRFSKEYPQRYFDVAIAEQHAVTLAAGMATQGAKPVVAIYSTFLQRGYDQLVHDVAVQQLDVLFAIDRGGVVGPDGATHAGNLDLSFLRCVPHMVVMAPADEAECRQMLSTGMQYQGPAAVRYPRGTGPGAALDSSLATLPIGKAQLRHSGTRIALLGFGATVDAAEAVGRDLGLTVVNMRFVKPLDKAMLLELAKTHEGFVTIEDNVVAGGAGSGVSELLNAEAITLPMLHLGLPDSFQHHASREDLLAEAGIDQAGIRTAVLKRWPQLMTGKTPSLNAAAG
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q2P472
|
P45110
|
ARGR_HAEIN
|
Arginine repressor
|
Haemophilus
|
MTENLTRAFKELLNQERFGSQSEIVDALKKQGFTGINQSKISRMLSKFGAVRTRNTKMEMVYCLPNELSVPNTSSPLKNLVLDVDHNAMLIVIKTTPGAAQLIARLLDSIGKSEGILGTIAGDDTIFVTPTNNKPIDELLQNIQRLFENTL
|
Regulates arginine biosynthesis genes.
|
P45110
|
P40684
|
DCUA_SERMA
|
C4-dicarboxylate transporter DcuA
|
Serratia
|
MLAVELVIVLLAIFLGARLGGIGIGFAGGLGVLALALIGVKPGNIPFDVISIIMAVIAAISAMQVAGGMDYLVQQTEKLLRKNPKHITILAPIVTYFLTIFAGTGNISLSALPVIAEVAKEQGIKPCRPLST
|
Responsible for the transport of C4-dicarboxylates during aerobic and anaerobic growth. Required for the uptake of L-aspartate as a nitrogen source during aerobic growth. The uptake of L-aspartate in aerobic conditions is coupled to the excretion of fumarate, resulting in the net uptake of nitrogen without carbon uptake. In addition, during anaerobic growth, catalyzes the uptake of fumarate, malate or aspartate coupled to the export of succinate. May play a a general role in anaerobic C4-dicarboxylate transport.
|
P40684
|
Q5GFD9
|
IMPCT_RAT
|
Imprinted and ancient gene protein homolog
|
Rattus
|
MAEVESGSNQRQNEEIEAMAAIYGEEWCVIDEVAKIFCIRITDDMDDPKWTLCLQVMLPSEYPGTAPPVYQLNAPWLKGQERAELAKSLEEIYMKNIGESILYQWVEKIRDALIQKSQITEPGPDEKKKTEEEEVEGEDDPILEHPPENPVKTWDLKISESAPEAEELPPIAHGAPITDRRSTFQAHLAPVVCIDQVKKVLAKLYENKKIASATHNIYAYRIYCEDKQTFLQDSEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNSPEESAKSFGKKKVKKDKKKGDH
|
Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.
|
Q5GFD9
|
A4Y6B8
|
GLO2_SHEPC
|
Glyoxalase II
|
Shewanella
|
MLTITAIKAFNDNYIWVLQQTPHSQVYVVDPGDAKVVIAYLVSHQLALAGILLTHHHQDHTGGVGELKRYVEQTSSQTLQVYGPQKENIAHVNVPLNPEMRTELTLPFLNAQIQVLNVPGHTAGHIAYFIEDALFCGDTLFSAGCGRLFEGTAEQMLSSLTLLAKLPANTRVFCAHEYTLSNLKFALTVEPNNLNLQAYMQKATEMRAQNSATIPSSIALERAINPFLRVGEQSIIDSIKQHFDDPDPIKLDELTCFTRLRQWKDIF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
A4Y6B8
|
Q2N908
|
TAL_ERYLH
|
Probable transaldolase
|
Erythrobacter
|
MQFFADTAEIDDIKELAATGLLDGVTTNPSLIHKSGRDFIEVTKEICGITDGPVSAEVVALDHATMMKEADKLRAIADNVCIKVPLTIDGLKTCKALSDDGTMVNVTLCFSANQALLAAKAGATFVSPFVGRHDDNGFNGMELIRDIRTIYDNYAFETEILVASVRHTTHVLEAALIGADVMTAPPKVIMALANHVLTNKGIEGFLKDWEATGQSIL
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q2N908
|
Q39262
|
ZFP3_ARATH
|
Zinc finger protein 3
|
Arabidopsis
|
MDASIVSSSTAFPYQDSLNQSIEDEERDVHNSSHELNLIDCIDDTTSIVNESTTSTEQKLFSCNYCQRTFYSSQALGGHQNAHKRERTLAKRGQRMAASASAFGHPYGFSPLPFHGQYNNHRSLGIQAHSISHKLSSYNGFGGHYGQINWSRLPFDQQPAIGKFPSMDNFHHHHHQMMMMAPSVNSRSNNIDSPSNTGRVLEGSPTLEQWHGDKGLLLSTSHHEEQQKLDLSLKL
|
Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development. Involved in the regulation of vegetative development and fertility. Modulates red light signaling in seedling photomorphogenesis.
|
Q39262
|
Q21252
|
NAS3_CAEEL
|
Nematode astacin 3
|
Caenorhabditis
|
MYRFIIFFSLLALTASKVSEPEKDDEIAVKIPTKRSVSEPPKDDDIAVKIPMRKKRGIAIHPWQWESHLWPNAEVPYDIASHYTATERGIILSAMEAFRDVTCVRFRPRRSTDKHYLQINKHYQLERCFSYIGRQSSRWLFGTRDGKVETRMKLDPSCLLYNGRGTVMHELMHILGFYHEHQRDDRDRRIGGSASHYNFKIYQRAKSYYMGGYDANSIMHYNFGSVPWQKRDYFSPSDIRNINTLYKCNNRVVSKFPSTIPSTSTTTTKAPQFELFEKKQIESNSLFRRRRS
|
Metalloprotease.
|
Q21252
|
Q7VYU0
|
CRCB_BORPE
|
Putative fluoride ion transporter CrcB
|
Bordetella
|
MLTYAPLNFIAIGIGATLGAWLRWVLGLRLNGAGWPWGTLTANLVGGYLIGVMVALIASHPEWPAWIRLAAVTGFLGGLTTFSTFSAETVDMLERGVYATAAAYAGASLAGSLAMTGLGLATVRLLLR
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
Q7VYU0
|
Q753K4
|
SYF2_ASHGO
|
Pre-mRNA-splicing factor SYF2
|
Eremothecium
|
MGIEDINRRLRQLKKKRVDASIRNRKEAASEERARLAEGKPRVYSMAEEPADEAEADDTQSEQLKLLNYRIADYEKWDEKQKRHKQPSDGADLGELANSTYRSELHQLHRRGVVKGRATNGRISASGKVVLDDEPELVEKLAAAVQQTAKRRHEERQKKAAKDGGRATAGSLNDKNRHFNEKLDREFRKRGQ
|
Involved in pre-mRNA splicing.
|
Q753K4
|
B1GZ94
|
RL24_ENDTX
|
50S ribosomal protein L24
|
Endomicrobium
|
MLNIKKKDKVLILSGKDRGKKGEVIYVSPDKGKVIVTKINVVKRHTNPTRKDLGGIHKKEAPIAISKIMLICPKCSRGSRAKFDKLSDGKKIRVCRRCGEVIV
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
B1GZ94
|
Q6F7S4
|
RL5_ACIAD
|
50S ribosomal protein L5
|
Acinetobacter
|
MARLKTRYNEELKAKLQQELGIKNVMEIPRITKITLNMGVGAAATDKKLLDGAVADMQLIAGQKPVVTLARKSIAGFKIRDGWPIGCKVTLRGEQMYEFLDRLISIAIPRIRDFRGFSSKSFDGRGNYSMGLKEQIVFPEIDFDKIDRIRGMDITITTTARTDDEGRALMRTFGFPFK
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q6F7S4
|
Q2NRL9
|
LPXA_SODGM
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Sodalis
|
MIDQSAFIHPSAIVEDGAIIHADVHVGPFCVIGPQVEIGARTVLESHVVVTGITRIGEDNQIYPFASLGDVNQDLKYAGEPTRVEIGHRNRIRESVTIHRGTIQGGEVTRVGSDNLLMVNAHVAHDCTVGSHCIMANNATLGGHVAVDDYAIIGGMTAVHQFCVIGAYVMVGGCSGVAQDVPPFVIAQGNHATPFGLNIEGLKRRGFDHAALHAIRAAYKIIYRSGKTLDEAKPELQALAQEHQVVNTFLDFLLRSQRGIIR
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q2NRL9
|
Q5V0E6
|
QUEC_HALMA
|
PreQ(0) synthase
|
Haloarcula
|
MTDDTRAVVLASGGMDSATAAYEAQTRGYDHLYLLHTSYGQNTEDREYECASALADHVDAADFLHVETGHLTQIGASSLTDDSMEVADADTDSDEIPTSYVPFRNANLLSMAVSYAEANDCGAVFIGAHSEDFSGYPDCRPAFFDAFQGVIDAGTKPDTDIALVAPFVEWSKTDIAERGVELGVPYADTWSCYRDDEPACGTCDACAFRLEAFQRIGERDPIEYAERPTYAE
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
Q5V0E6
|
B5EFQ9
|
RS17_CITBB
|
30S ribosomal protein S17
|
Citrifermentans
|
MSERGNRKTQVGVVVSDKMDKTAVVKVDRLVKHPVYNKYIKRSAKYKAHDMDNAAKIGDRVLIVETRPLSKDKRWKIRQIIESKG
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
B5EFQ9
|
B1J5G5
|
MTNA_PSEPW
|
S-methyl-5-thioribose-1-phosphate isomerase
|
Pseudomonas
|
MRERLMAAEKVTGIRWHHGALHLLDQRLLPSQERWLACDNVAQVAAAIRDMAVRGAAAIGIAAAYGLVLALEERLAEGGDWEMDLEEDFLSLAEARPTAANLFWALNRMRDRLQRLRPGEDVLAALEAEAVAIHESDREANLTMAQQGIELIRRHQGSEQALLTYGNAGALASGGFGTALGVIRAGFLEGMVERVYAGETRPWLQGSRLTAWELANEGIPVTLCADSALAHLMKSKGITWVVVGADCIAANGDVASKIGTYQLAVNAMHHGVRFMVVAPSTSIDLNLATGEDIPLEERDADELLDYAGTRVAPQVEVFNPVFDVTPADLIDVIVTEKGVIERPDTAKLAQLMCRKRLH
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
B1J5G5
|
O51742
|
RBFA_BORBU
|
Ribosome-binding factor A
|
Borreliella
|
MYKNIKKFKLESFIAQEIGNLIVSGGIKDPRIHSFLTVVKVEFSKDLINAKVFMGSIKEGASLDNAVKALNNAKGFIQSQIIKRIKVRSTPKLLFVKDDSLSKSFYVNKLIEGLNTTREN
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
O51742
|
Q59RL7
|
CPH2_CANAL
|
Candida pseudohyphal regulator 2
|
Candida
|
MLSQYDEQLAAGDNNGFNKQGNATLYSFDFVDADDFLDSISGALPNNGHNNVNPNTNDISFEDMNIMNPNIYSPVSAASGDDFTQSSGQPMISEGSNYTGQNFTDYLSDNSLEGYDKNTSRPLHEVDIGFSNKRSNSTSTGSLSHNEEITPISHYSVDSIVTSPEPPINKQGDFPPIKRTTTVSSTNSITNTTKKPAKVTKPKSKDKNSHNMIEKKYRTNINTKILALRDAVPALRIAAGCDDVSIADLEGLTPASKLNKASVLTKATEYIKHLESKNFILKQQNIELHRLIQHANMNPKSLPPPPQQMQAPPQPGFGFYPPQNQSFNVTPASQYPSPQQQVSPTQQQTVHHPPQPNRYLLGGMAAVMGTSLFGGSGENDFRSLSALPFSYLFPNAILNPSPLTIQLWTLTKVLLVVGSLASIFIPMYKQAQLKKEDKPNTIPETSLLDWILISIGFKTPAKLSVSKRDAIISNLQGGNDWSQLVSDYFYLAGCEINFENCFLSLVLGTIIRHRFPVVATILNHYLSMKEALLLNLDYKGFSKSLIRLNQLISKVDGVSIFESTNLTTRLTNVFTNNRINANIVDGQNHVKYIEFYQRNINDYYAIVFNWRLLEFIHELNVTYLEQLNDDQSQVLTDLKIIEAFFGEQDNKLFGYYQLFTSILNANYAPYLFESLKDKVESSLEKFRIAYEGIDLTDHEIHNTSSEDEYEQESPVVYKYEPTLKSQKSLISSLNLVNEEEFIILTCSLTIYYYKNKEYDRALKLLNYLRLDNDSKTLSLLTFTSLITLINELIPGKIEDNVNLDSAIRICRDWLENPDLTQYMDEDIKLELKKIVVTKGMIVNGIDVNESDEE
|
Transcription factor that positively controls filamentous growth, virulence, and invasiveness. Binds directly to the two SRE-1-like elements upstream of TEC1 and thus regulates positively expression of this important hyphal growth regulator. Functions independently of known signaling cascades involving EFG1. Regulates also gene expression during intestinal colonization but is not involved in host cell adhesion.
|
Q59RL7
|
Q8VW75
|
COAD_PHODP
|
Pantetheine-phosphate adenylyltransferase
|
Photobacterium
|
MTTRVIYPGTFDPITNGHLDLIERAAAMFDTVIVGVAYNPTKKPLFDLNERVALAQSVTQHLPNVEIVGFSGLLVNFAKEHNANVLVRGLRAVSDFEYEFQLANMNRRLMPELETVFLTPAEENSFISSTIVKEVALHKGDVSQFVPNQISQALNKKLFA
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
Q8VW75
|
B9I2J6
|
AXEP_POPTR
|
L-Ala-D/L-Xxx epimerase
|
Populus
|
MLSIGSLCLSLGTTPKPLKPSKTPKPIRKLYATKAMAGSNPKQVSTFEFRDLMETFAVDVKRAENRPLNVPLIAPFTIASSRLDKVENVAIRIELSDGCVGWGEAPILPFVTAEDQSTAMIKAREACELLKNSSSMKLGLVLERVSEILPGHEFASVRAGVEMALIDAVAKSINVPLWILFGGASDSITTDITIPIVSSAEAAELASKYRKQGFQTLKLKVGKNLKEDIEVLQAIRAVHPDCLFILDANEGYKPEEAIEVLEELHKMGVTPILFEQPVHRDDWEGLGHVTHIAKGKYGVSVAADESCRSLVDAKRIIKGNLADVINIKLAKVGVVGGLEIIEEARTSGLDLMIGGMVETRLAMGFAGHLAAGFGCFKFIDLDTPLLLSEDPVLEGYEVSGAVYKFTDAQGHAGFLDWDNVL
|
Catalyzes the epimerization of various hydrophobic and polar dipeptides. Has epimerase activity with L-Ala-L-Ala, L-Ala-L-Ser, L-Ala-L-Thr and L-Ala-L-Trp (in vitro).
|
B9I2J6
|
B3VMC0
|
BADH2_ORYSI
|
Betaine aldehyde dehydrogenase 2
|
Oryza sativa
|
MATAIPQRQLFVAGEWRAPALGRRLPVVNPATESPIGEIPAGTAEDVDAAVAAAREALKRNRGRDWARAPGAVRAKYLRAIAAKIIERKSELARLETLDCGKPLDEAAWDMDDVAGCFEYFADLAESLDKRQNAPVSLPMENFKCYLRKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADVCKEVGLPSGVLNIVTGLGSEAGAPLSSHPGVDKVAFTGSYETGKKIMASAAPMVKPVSLELGGKSPIVVFDDVDVEKAVEWTLFGCFWTNGQICSATSRLILHKKIAKEFQERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKQFVSTAKSQGATILTGGVRPKHLEKGFYIEPTIITDVDTSMQIWREEVFGPVLCVKEFSTEEEAIELANDTHYGLAGAVLSGDRERCQRLTEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYASDEPWGWYKSPSKL
|
Dehydrogenase that can use N-acetyl-c-aminobutyraldehyde (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4-aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N-trimethylaminobutyraldehyde (TMAB-ald) and 3-N-trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the oxidation of GAB-ald more efficiently than Bet-ald. Mediates the conversion of GAB-ald into gamma-aminobutyric acid (GABA), and prevents the formation of 2-acetyl-1-pyrroline (2AP) which gives fragrant rice its aromatic properties.
|
B3VMC0
|
B7J440
|
NRDR_ACIF2
|
Transcriptional repressor NrdR
|
Acidithiobacillus
|
MHCPFCAYADTRVVDSRLADDGGSVRRRRECPQCGQRFTTFERAELALPVVVKTDGRRESFNEEKLQRGLTRALSKRPVATARVDAAVRMIQRRIRERGEREIPARLIGELVMEALRDLDPVAYVRFASVYRRFEDVDAFSVEIARMKEAEVPDGGDDLNRGD
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
B7J440
|
Q9WY79
|
MURE_THEMA
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Thermotoga
|
MNISTIVSNLKDLILEVRAPYDLEITGVSNHSSKVKKGDLFICRRGEKFDSHEIIPEVMEKGAVAVVVEREIDLDFPYIQVFDSRYFEAKVASLFFEDPWKDVLTFGVTGTNGKTTTTMMIYHMLTSLGERGSVLTTAVKRILGNSYYDDITTPDAITILSAMKENREGGGKFFALEVSSHALVQQRVEGVRFDVGIFTNISRDHLDFHGTFENYLKAKLHLFDLLKDDGVAVLNESLADAFNRKSRKITFGTSKNADYRLGNIEVSWEGTQFVLETPDGLLKVFTRAIGDFNAYNAAAAIAALHQLGYDPKDLASSLETFTGVEGRFEVVRGAKKIGLNVVVDFAHSPDALEKLLKNVRKISQGRVIVVFGAGGNSDRGKRPMMSEVASKLADVVILTTDDPRGEDPEQIMEDLIKGIDKRKPYLVLFDRREAIETALTIANRGDSVVIAGRGHERYQIIDEEKKVPFQDREVVEEIIRDKLKGRKYAQ
|
Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently.
|
Q9WY79
|
B2SCZ4
|
CH60_BRUA1
|
Chaperonin-60
|
Brucella
|
MAAKDVKFGRTAREKMLRGVDILADAVKVTLGPKGRNVVIEKSFGAPRITKDGVSVAKEVELEDKFENMGAQMLREVASKTNDTAGDGTTTATVLGQAIVQEGAKAVAAGMNPMDLKRGIDLAVNEVVAELLKKAKKINTSEEVAQVGTISANGEAEIGKMIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQALLPVLEAVVQTSKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGQVISEDLGIKLESVTLDMLGRAKKVSISKENTTIVDGAGQKAEIDARVGQIKQQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALNATRAAVEEGIVAGGGTALLRASTKITAKGVNADQEAGINIVRRAIQAPARQITTNAGEEASVIVGKILENTSETFGYNTANGEYGDLISLGIVDPVKVVRTALQNAASVAGLLITTEAMIAELPKKDAAPAGMPGGMGGMGGMDF
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
B2SCZ4
|
P26350
|
PTMA_MOUSE
|
Thymosin alpha
|
Mus
|
MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVDTKKQKTEEDD
|
Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
|
P26350
|
Q1E0G9
|
EFG1P_COCIM
|
rRNA-processing protein EFG1
|
Coccidioides
|
MSLHEPEAQPSLKKRRRDSFSNADPKRVKRLHSGTQRLHYHDIGPSVNELKTRIRDVKRLLAKRIDDLPADVRVAKERELAECQRDLEKAEVKKQRSKMIQKYHFVRFLERKRATKELKRLKGQLHKLENDDRLDPNARENSIETLNRKISASEIDLNYTIYSPLTEKYISLYPNERRKQQPMEPEESNVIRTNSGEKPPLWYTVKQSMADGTLELLRDGKLGIGLSGEKKDSNNADVSLKSNTMSLLVHRKQKKPKSKIKVDGDEDAKRSSARSVQEGTRNENKRTSKEDVQGEDDDAESESDGGFFE
|
Involved in rRNA processing.
|
Q1E0G9
|
Q82IY7
|
PTLD_STRAW
|
Neopentalenolactone biosynthesis protein D
|
Streptomyces
|
MSRAMDITRIPGSAIGAVVAGADFSGTIDDTQVEEIWQALDQHLVLVFRGHKDPSNDDLLMFARRFGHVPKTGLTTGASPDHNEILLISNILDENGQKIGVGNAEWMDWHTDYSFRPRVSRIGFLAAVELPPSGGGQTLFTDMYTAYESLPDDLRQRLHSYRARHSLRSGYEDVIEEEYQGEVSIEGPTAKPFVAPEDGTATVHQLIARNPRTGRRAVYANPLNTKRILELDVTSSKEVLQQLFAKPGEPELTYAHEWLPGDIVMWDQLGTVHAKRAFDPTERRLLRKVVTIFDDPAEPWHPEDAA
|
Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F. Also able to catalyze the oxidation of pentalenolactone D to pentalenolactone E. In presence of neopentalenolactone D, mediates production of PL308 and possibly neopentalenolactone E.
|
Q82IY7
|
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